References of "Sluse, Francis"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailPhylogenetic classification of the mitochondrial carrier family of Saccharomyces cerevisiae.
Elmoualij, Benaïssa ULg; Duyckaerts, Claire ULg; Brasseur, Josette ULg et al

in Yeast (Chichester, England) (1997), 13(6), 573-581

The screening of the open reading frames identified in the whole yeast genome has allowed us to discover 34 proteins belonging to the mitochondrial carrier family. By phylogenetic study, they can be ... [more ▼]

The screening of the open reading frames identified in the whole yeast genome has allowed us to discover 34 proteins belonging to the mitochondrial carrier family. By phylogenetic study, they can be divided into 27 subfamilies including ADP/ATP, phosphate and citrate carriers, putative oxoglutarate and GDC carriers and 22 new subfamilies. Topology predictions using the 'positive inside rule' approach have shown that the yeast carriers are similarly oriented with both extremities exposed to the cytosol. In each subfamily, a strict conservation of the charged residues in the six transmembrane alpha-helices is observed, suggesting a functional role for these residues and the existence of 27 functionally distinct carriers. [less ▲]

Detailed reference viewed: 127 (11 ULg)
Full Text
Peer Reviewed
See detailReversibility of thiamine deficiency-induced partial necrosis and mitochondrial uncoupling by addition of thiamine to neuroblastoma cell suspensions.
Bettendorff, Lucien ULg; Goessens, Guy ULg; Sluse, Francis ULg

in Molecular and Cellular Biochemistry (1997), 174(1-2), 121-4

Culture of neuroblastoma cells in the presence of low thiamine concentration (16 nM) and of the transport inhibitor amprolium leads to the appearance of signs of necrosis: the chromatin condenses, the ... [more ▼]

Culture of neuroblastoma cells in the presence of low thiamine concentration (16 nM) and of the transport inhibitor amprolium leads to the appearance of signs of necrosis: the chromatin condenses, the oxygen consumption decreases and is uncoupled, the mitochondrial cristae are disorganized, the thiamine diphosphate-dependent dehydrogenase activities are impaired. When 10 microM thiamine are added to these cells, the basal respiration increases, the coupled respiration is restored and mitochondrial morphology is recovered within 1 h. Addition of succinate, which is oxidized via a thiamine diphosphate-independent dehydrogenase, to digitonin-permeabilized cells immediately restores a coupled respiration. Our results suggest that the slowing of the citric acid cycle is the cause of the biochemical lesion induced by severe thiamine deficiency and that part of the mitochondria remain functional. [less ▲]

Detailed reference viewed: 31 (17 ULg)
Full Text
Peer Reviewed
See detailElectron partitioning between the two branching quinol-oxidizing pathways in Acanthamoeba castellanii mitochondria during steady-state state 3 respiration.
Jarmuszkiewicz, W.; Sluse-Goffart, C.; Hryniewiecka, L. et al

in Journal of Biological Chemistry (1997), 273(17), 10174-10180

Amoeba mitochondria possess a respiratory chain with two quinol-oxidizing pathways: the cytochrome pathway and the cyanide-resistant alternative oxidase pathway. The ADP/O method, based on the non ... [more ▼]

Amoeba mitochondria possess a respiratory chain with two quinol-oxidizing pathways: the cytochrome pathway and the cyanide-resistant alternative oxidase pathway. The ADP/O method, based on the non-phosphorylating property of alternative oxidase, was used to determine contributions of both pathways in overall state 3 respiration in the presence of GMP (an activator of the alternative oxidase in amoeba) and succinate as oxidizable substrate. This method involves pair measurements of ADP/O ratios plus and minus benzohydroxamate (an inhibitor of the alternative oxidase). The requirements of the method are listed and verified. When overall state 3 respiration was decreased by increasing concentrations of n-butyl malonate (a non-penetrating inhibitor of succinate uptake), the quinone reduction level declined. At the same time, the alternative pathway contribution decreased sharply and became negligible when quinone redox state was lower than 50%, whereas the cytochrome pathway contribution first increased and then passed through a maximum at a quinone redox state of 58% and sharply decreased at a lower level of quinone reduction. This study is the first attempt to examine the steady-state kinetics of the two quinol-oxidizing pathways when both are active and to describe electron partitioning between them when the steady-state rate of the quinone-reducing pathway is varied. [less ▲]

Detailed reference viewed: 14 (4 ULg)
Full Text
Peer Reviewed
See detailType II to type I transformation of chronically stimulated goat latissimus dorsi muscle: a histoenzymological, biochemical, bioenergetic, and functional study.
Radermacker, M. A.; Focant, B.; Hautecler, T. et al

in European Surgical Research = Europäische Chirurgische Forschung = Recherches Chirurgicales Européennes (1996), 28

Five goat latissimus dorsi muscles (LDM) were submitted to a progressive chronic electrostimulation program to reach an integrated understanding of the fast-to-slow transformation process in large mammals ... [more ▼]

Five goat latissimus dorsi muscles (LDM) were submitted to a progressive chronic electrostimulation program to reach an integrated understanding of the fast-to-slow transformation process in large mammals. LDM were regularly sampled and followed during a period of 8 months. Each sample was simultaneously assessed for histoenzymological study, myosin and LDH isoforms and bioenergetic capacities [NADH dehydrogenase cytochrome c oxidoreductase (NADH Cyt c OR), succinate dehydrogenase cytochrome c oxidoreductase (Succ Cyt c OR), cytochrome c oxidase (Cyt c Ox) and LDH]. Such muscles were also tested with and without completion of II to I transformation for their mechanical properties in isometric and isotonic strain gauge testing. The conversion of fast-to-slow myosin monitored by heavy chain (HC I) and light chain slow component (LC2s) began a few days after stimulation and was almost 100% after 100 days. The H-LDH isoforms evolved similarly but did not reach 100% conversion after 200 days. The activity of respiratory chain oxidases increased within 36 h but to a variable extent and peaked after 32 days, corresponding to a 75% transformation of myosin compared to initial levels. NADH Cyt c OR, Succ Cyt c OR, and Cyt c Ox, respectively increased 10-, 5- and 5-fold. These activities then significantly decreased before the completion of the myofibrillar transformation and reached a plateau with stable activities that remained 2- to 3-fold higher than the unstimulated LDM. LDH activity sharply decreased until day 62 (5-fold) and then plateaued. Functionally, muscle showed a reduced speed of contraction and moderate reduction in power output but had become fatigue-resistant. This study documents the transformation process in large mammals and suggests the dynamic relation between workload, aerobic-anaerobic metabolism and the contractile myofibrillar system. [less ▲]

Detailed reference viewed: 18 (7 ULg)
Full Text
See detailMitochondrial oxidative phosphorylation : in vitro and in situ effect of EGb 761
Willet, K.; DETRY, Olivier ULg; Evens, A. et al

in Packer, L.; Trabet, Maret G; Xin, Wenjuan (Eds.) Proceedings of the international symposium on natural antioxidants molecular mechanisms and health effects (1996)

Detailed reference viewed: 7 (4 ULg)
Full Text
See detailInitial rate study of [C14]ADP uptake in ADP loaded mitoplasts and the kinetic mechanism of the ADP/ATP carrier
Sluse-Goffart, C.; Evens, A.; Duyckaerts, Claire ULg et al

in WEsterhoff, H. V.; Snoep, J.; Wijker, J. (Eds.) et al Biothermokinetics of the living cell (1996)

Detailed reference viewed: 14 (1 ULg)
Full Text
See detailDetermination of the respective contributions of the cytochrome and alternative oxidase pathway in Acanthamoeba catellanii
Jarmuszkiewicz, W.; Sluse-Goffart, C.; Hryniewiecka, L. et al

in Westerhoff, H.; Snoep, J.; Sluse, Francis (Eds.) et al Biothermokinetics of the living cell (1996)

Detailed reference viewed: 7 (1 ULg)
Full Text
See detailRedox state behavior of membrane ubiquinone 9 and exogenos ubiquinone 2 determined by HPLC during respiration of Chlamydomonas reinhardtii mitochondria.
T'serstevens, B.; Sluse-goffart, C.; Duyckaerts, Claire ULg et al

in Westerhoff, H.; Snoep, J.; Sluse, Francis (Eds.) et al Biothermokinetics of the living cell (1996)

Detailed reference viewed: 16 (3 ULg)
Full Text
See detailBiothermokinetics of the living cell
Westerhoff, H.; Snoep, J.; Sluse, Francis ULg et al

Book published by Biothermokinetics (1996)

Detailed reference viewed: 31 (1 ULg)
Full Text
Peer Reviewed
See detailMitochondrial metabolite carrier family, topology, structure and functional properties: an overview.
Sluse, Francis ULg

in Acta Biochimica Polonica. Polish. (1996), 43(2), 349-360

A set of metabolite carriers operates the traffic of numerous molecules consumed or produced in mitochondrial matrix and/or cytosolic compartments. As their existence has been predicted by the ... [more ▼]

A set of metabolite carriers operates the traffic of numerous molecules consumed or produced in mitochondrial matrix and/or cytosolic compartments. As their existence has been predicted by the chemiosmotic theory, the first challenge, in the late sixties, was to prove their presence in the inner mitochondrial membrane and to describe the various transports carried out. The second challenge was to understand their mechanisms by the kinetic approach in intact mitochondria (seventies). The third challenge (late seventies-eighties) was to isolate and to reconstitute the carriers in liposomes in order to characterize the proteins and to establish the concept of a structural and a functional family as well as some structure-function relationship with the help of primary sequences. Genetics, molecular biology and genomic sequencing bring the fourth challenge (nineties): a raising number of putative carriers becomes known only by their primary sequences but their functions have to be discovered. The actual challenge of the future is the elucidation of the ternary structure of carrier proteins that together with site-directed mutagenesis and kinetic mechanism will permit to advance in the understanding of molecular mechanisms of transport processes. [less ▲]

Detailed reference viewed: 17 (4 ULg)
Full Text
Peer Reviewed
See detailMutations Affecting the Mitochondrial Genes Encoding the Cytochrome Oxidase Subunit I and Apocytochrome B of Chlamydomonas Reinhardtii
Colin, Martine ULg; Dorthu, M. P.; Duby, Franceline ULg et al

in Molecular & General Genetics [=MGG] (1995), 249(2), 179-84

Mitochondrial mutants of the green alga Chlamydomonas reinhardtii that are inactivated in the cytochrome pathway of respiration have previously been isolated. Despite the fact that the alternative oxidase ... [more ▼]

Mitochondrial mutants of the green alga Chlamydomonas reinhardtii that are inactivated in the cytochrome pathway of respiration have previously been isolated. Despite the fact that the alternative oxidase pathway is still active the mutants have lost the capacity to grow heterotrophically (dark + acetate) and display reduced growth under mixotrophic conditions (light + acetate). In crosses between wild-type and mutant cells, the meiotic progeny only inherit the character transmitted by the mt- parent, which indicates that the mutations are located in the 15.8 kb linear mitochondrial genome. Two new mutants (dum-18 and dum-19) have now been isolated and characterized genetically, biochemically and at the molecular level. In addition, two previously isolated mutants (dum-11 and dum-15) were characterized in more detail. dum-11 contains two types of deleted mitochondrial DNA molecules: 15.1 kb monomers lacking the subterminal part of the genome, downstream of codon 147 of the apocytochrome b (COB) gene, and dimers resulting from head-to-head fusion of asymmetrically deleted monomers (15.1 and 9.5 kb DNA molecules, respectively). As in the wild type, the three other mutants contain only 15.8 kb mitochondrial DNA molecules. dum-15 is mutated at codon 140 of the COB gene, a serine (TCT) being changed into a tyrosine (TAC). dum-18 and dum-19 both inactivate cytochrome c oxidase, as a result of frameshift mutations (addition or deletion of 1 bp) at codons 145 and 152, respectively, of the COX1 gene encoding subunit I of cytochrome c oxidase. In a total of ten respiratory deficient mitochondrial mutants characterized thus far, only mutations located in COB or COX1 have been isolated.(ABSTRACT TRUNCATED AT 250 WORDS) [less ▲]

Detailed reference viewed: 31 (4 ULg)
See detailLocalization and transmembrane topology of a new member of the mitochondrial carrier family, the yeast RIM 2 gene product
Elmoualij, Benaïssa ULg; Duyckaerts, Claire ULg; Lamotte-Brasseur, J. et al

in Archives Internationales de Physiologie, de Biochimie et de Biophysique (1995)

Detailed reference viewed: 23 (9 ULg)
Full Text
Peer Reviewed
See detailMitochondrial oxidative phosphorylation injuries occurring in situ and in vitro.
Willet, K.; Vaz de Macedo, D.; DETRY, Olivier ULg et al

in Transplantation Proceedings (1995), 27

Detailed reference viewed: 15 (3 ULg)
Full Text
Peer Reviewed
See detailThiamine Deficiency--Induced Partial Necrosis and Mitochondrial Uncoupling in Neuroblastoma Cells Are Rapidly Reversed by Addition of Thiamine
Bettendorff, Lucien ULg; Sluse, Francis ULg; Goessens, Guy ULg et al

in Journal of Neurochemistry (1995), 65(5), 2178-2184

Culture of neuroblastoma cells in a medium of low-thiamine concentration (6 nM) and in the presence of the transport inhibitor amprolium leads to the appearance of overt signs of necrosis; i.e., the ... [more ▼]

Culture of neuroblastoma cells in a medium of low-thiamine concentration (6 nM) and in the presence of the transport inhibitor amprolium leads to the appearance of overt signs of necrosis; i.e., the chromatin condenses in dark patches, the oxygen consumption decreases, mitochondria are uncoupled, and their cristae are disorganized. Glutamate formed from glutamine is no longer oxidized and accumulates, suggesting that the thiamine diphosphate-dependent alpha-ketoglutarate dehydrogenase activity is impaired. When thiamine (10 microM) is added to the cells, the O2 consumption increases, respiratory control is restored, and normal cell and mitochondrial morphology is recovered within 1 h. Succinate, which is oxidized via the thiamine diphosphate-independent succinate dehydrogenase, is also able to restore a normal O2 consumption (with respiratory control) in digitonin-permeabilized thiamine-deficient cells. Our results therefore suggest that the slowing of the citric acid cycle is the main cause of the biochemical lesion induced by thiamine deficiency as observed in Wernicke's encephalopathy. [less ▲]

Detailed reference viewed: 43 (24 ULg)
Full Text
Peer Reviewed
See detailThiamine Deficiency in Cultured Neuroblastoma Cells: Effect on Mitochondrial Function and Peripheral Benzodiazepine Receptors
Bettendorff, Lucien ULg; Goessens, Guy ULg; Sluse, Francis ULg et al

in Journal of Neurochemistry (1995), 64(5), 2013-2021

When neuroblastoma cells were transferred to a medium of low (6 nM) thiamine concentration, a 16-fold decrease in total intracellular thiamine content occurred within 8 days. Respiration and ATP levels ... [more ▼]

When neuroblastoma cells were transferred to a medium of low (6 nM) thiamine concentration, a 16-fold decrease in total intracellular thiamine content occurred within 8 days. Respiration and ATP levels were only slightly affected, but addition of a thiamine transport inhibitor (amprolium) decreased ATP content and increased lactate production. Oxygen consumption became low and insensitive to oligomycin and uncouplers. At least 25% of mitochondria were swollen and electron translucent. Cell mortality increased to 75% within 5 days. [3H]PK 11195, a specific ligand of peripheral benzodiazepine receptors (located in the outer mitochondrial membrane) binds to the cells with high affinity (KD = 1.4 +/- 0.2 nM). Thiamine deficiency leads to an increase in both Bmax and KD. Changes in binding parameters for peripheral benzodiazepine receptors may be related to structural or permeability changes in mitochondrial outer membranes. In addition to the high-affinity (nanomolar range) binding site for peripheral benzodiazepine ligands, there is a low-affinity (micromolar range) saturable binding for PK 11195. At micromolar concentrations, peripheral benzodiazepines inhibit thiamine uptake by the cells. Altogether, our results suggest that impairment of oxidative metabolism, followed by mitochondrial swelling and disorganization of cristae, is the main cause of cell mortality in severely thiamine-deficient neuroblastoma cells. [less ▲]

Detailed reference viewed: 28 (13 ULg)